Host defence peptides from invertebrates – emerging antimicrobial strategies

Hancock, Robert E. W.; Brown, Kelly L.; Mookherjee, Neeloffer

doi:10.1016/j.imbio.2005.10.017

Cited by 240 publications

(150 citation statements)

References 53 publications

(58 reference statements)

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“…[5][6][7] Owing to these activities, AMPs can act as a first line of defense against invading pathogens, and they are considered to be important components of the innate immune systems of various animal species. [8][9][10] The AMPs were initially identified during biochemical purification, whereas recently, more and more putative novel AMPs have been found by molecular biological techniques via expressed sequence tag analyses and gene cloning. 11,12 A putative AMP HKPLP consists of 24 amino-acid residues, which is encoded by a novel gene from the brooding pouch cDNA library of Hippocampus kuda Bleeker, a seahorse used as a traditional Chinese medicine.…”

Section: Introductionmentioning

confidence: 99%

Identification, synthesis and characterization of a novel antimicrobial peptide HKPLP derived from Hippocampus kuda Bleeker

Sun

Jing

et al. 2012

J Antibiot

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A novel gene encoding 55 amino-acid residues has been identified from the brooding pouch cDNA library of Hippocampus kuda Bleeker. The deduced amino-acid sequence is highly homologous to several pleurocidin-like peptides from the winter flounder and comprises a signal peptide, a pro-peptide and a mature peptide. The glycine-rich mature peptide, designated HKPLP, contains 24 amino-acid residues and has been synthesized by solid-phase peptide synthesis. The purified HKPLP exhibits antimicrobial activity against several Gram-positive and Gram-negative bacterial strains at low concentrations (MIC 1.5-7.5 lM). Thermal stability assay data show good heat stability. CD spectroscopy experiments indicate that the dominant contents are anti-parallel and parallel sheets, which may have b-sheet or b-strand motif. It is inferred that HKPLP participates in the host defense during egg fertilization and embryo development as an antimicrobial peptide in brooding pouch.

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Section: Introductionmentioning

confidence: 99%

Identification, synthesis and characterization of a novel antimicrobial peptide HKPLP derived from Hippocampus kuda Bleeker

Sun

Jing

et al. 2012

J Antibiot

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“…[1][2][3][4] They have emerged as a potential new class of antimicrobial agents with new modes of actions. 5 There are AMPs which are rich in a certain specific amino acid such as Pro, Trp, or Arg.…”

Section: Introductionmentioning

confidence: 99%

A Novel Trp-rich Model Antimicrobial Peptoid with Increased Protease Stability

Bang

Nan²,

Lee³

et al. 2010

Bulletin of the Korean Chemical Society

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In order to increase protease stability of a novel Trp-rich model antimicrobial peptide, K6L2W3 (KLWKKWKKWLK-NH2) and investigate the effect of L-amino acid to peptoid residue conversion on biological functions, we synthesized its antimicrobial peptoid, k6l2w3. Peptoid k6l2w3 had similar bacterial selectivity compared to peptide K6L2W3. The bactericidal rate of k6l2w3 was somewhat slower than that of K6L2W3. Peptoid k6l2w3 exhibited very little dye leakage from bacterial outer-membrane mimicking PE/PG liposomes, as observed in K6L2W3, indicating that the major target site of K6L2W3 and k6l2w3 may be not the cell membrane but the cytoplasm of bacteria. Trypsin treatment of K6L2W3 completely abolished antimicrobial activities against Escherichia coli and Staphylococcus aureus. In contrast, the antimicrobial activity of k6l2w3 was completely preserved after trypsin treatment. Taken together, our results suggested that antimicrobial peptoid k6l2w3 can potentially serves as a promising therapeutic agent for the treatment of microbial infection.

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“…Two promising families of drugs that meet these criteria are host-defense cationic antimicrobial peptides (AMPs) and lipopeptides. AMPs are produced by all species of life and represent key components of the innate immune system, providing a fast acting weapon against invading pathogens including bacteria, fungi, and yeast (1)(2)(3)(4). Importantly, many AMPs physically and rapidly permeate and destroy the cell membrane, causing damage hard to fix, in contrast to conventional antibiotics, which act on specific targets such as enzymes or DNA.…”

mentioning

confidence: 99%

Ultrashort antibacterial and antifungal lipopeptides

Makovitzki

Avrahami

Shai

2006

Proc. Natl. Acad. Sci. U.S.A.

425

392

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Host-defense cationic antimicrobial peptides (Ϸ12-50 aa long) play an essential protective role in the innate immune system of all organisms. Lipopeptides, however, are produced only in bacteria and fungi during cultivation, and they are composed of specific lipophilic moieties attached to anionic peptides (six to seven amino acids). Here we report the following. (i) The attachment of an aliphatic chain to otherwise inert, cationic D,L tetrapeptides endows them with potent activity against various microorganisms including antibiotic resistance strains. (ii) Cell specificity is determined by the sequence of the short peptidic chain and the length of the aliphatic moiety. (iii) Despite the fact that the peptidic chains are very short, their mode of action involves permeation and disintegration of membranes, similar to that of many long antimicrobial peptides. Besides adding important information on the parameters necessary for host-defense lipopeptides to kill microorganisms, the simple composition of these lipopeptides and their diverse specificities should make them economically available, innate immunity-mimicking antimicrobial and antifungal compounds for various applications.antimicrobial peptides ͉ innate immunity ͉ peptide-membrane interaction ͉ carpet model ͉ lytic peptides

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Host defence peptides from invertebrates – emerging antimicrobial strategies

Cited by 240 publications

References 53 publications

Identification, synthesis and characterization of a novel antimicrobial peptide HKPLP derived from Hippocampus kuda Bleeker

Identification, synthesis and characterization of a novel antimicrobial peptide HKPLP derived from Hippocampus kuda Bleeker

A Novel Trp-rich Model Antimicrobial Peptoid with Increased Protease Stability

Ultrashort antibacterial and antifungal lipopeptides

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